Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

CO2 reduction to the level of formylmethanofuran in Methanosarcina barkeri is non-energy driven when CO is the electron donor.

FEMS microbiology letters - 1 Jun 2004

Stojanowic Alexander, Hedderich Reiner

Abstract excerpt

A Methanosarcina barkeri mutant lacking Ech hydrogenase does not catalyze CH(4) formation from H(2)/CO(2) since, as was shown previously, the energy-driven reduction of CO(2) to formylmethanofuran by H(2) is blocked. CH(4) formation by this mutant could be restored in the presence of CO or pyruvate. Furthermore, CH(4) formation from H(2)/CO(2) plus CO by the Deltaech mutant was not inhibited by the protonophore...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Carbon Dioxide
Share to Carbon Monoxide
Share to Deuterium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electrons

Share to Furans

Share to Methane

Share to Oxidoreductases

Share to Pyruvic Acid

Source

Identifiers

PMID: 15158277
DOI: 10.1016/j.femsle.2004.04.028

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

CO2 reduction to the level of formylmethanofuran in Methanosarcina barkeri is non-energy driven when CO is the electron donor.PMID 15158277Read ↗

Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation.Semantic proximity Read ↗

Hydrogen is a preferred intermediate in the energy-conserving electron transport chain of Methanosarcina barkeri.Semantic proximity Read ↗

Genetic, Biochemical, and Molecular Characterization of Methanosarcina barkeri Mutants Lacking Three Distinct Classes of Hydrogenase.Semantic proximity Read ↗

Role of a putative tungsten-dependent formylmethanofuran dehydrogenase in Methanosarcina acetivorans.Semantic proximity Read ↗

Function of Ech hydrogenase in ferredoxin-dependent, membrane-bound electron transport in Methanosarcina mazei.Semantic proximity Read ↗

Essential anaplerotic role for the energy-converting hydrogenase Eha in hydrogenotrophic methanogenesis.Semantic proximity Read ↗

Redirecting electron flow in Acetobacterium woodii enables growth on CO and improves growth on formate.Semantic proximity Read ↗

The Rnf Complex Is an Energy-Coupled Transhydrogenase Essential To Reversibly Link Cellular NADH and Ferredoxin Pools in the Acetogen Acetobacterium woodii.Semantic proximity Read ↗

Loss of the <i>mtr</i> operon in <i>Methanosarcina</i> blocks growth on methanol, but not methanogenesis, and reveals an unknown methanogenic pathwaySemantic proximity Read ↗

The effect of a C298D mutation in CaHydA [FeFe]-hydrogenase: Insights into the protein-metal cluster interaction by EPR and FTIR spectroscopic investigation.Semantic proximity Read ↗

Mutagenesis of the C1 oxidation pathway in Methanosarcina barkeri: new insights into the Mtr/Mer bypass pathway.Semantic proximity Read ↗

[Energy transformation coupled to formate oxidation during anaerobic fermentation].Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.